id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-004592-a3k56ulv	Liu, Xiaoju	SUMO fusion system facilitates soluble expression and high production of bioactive human fibroblast growth factor 23 (FGF23)	2012-01-17		.txt	text/plain	5280	260	52	To prepare soluble and bioactive recombinant human FGF23 to meet the increasing demand in its pharmacological application, small ubiquitin-related modifier (SUMO)-FGF23 fusion gene and FGF23 non-fusion gene were amplified by standard PCR methods and cloned into vector pET-22b and pET-3c, then transformed into Escherichia coli Rosetta (DE3) and BL21 (DE3). An analysis was performed to determine the effects of the three factors (IPTG concentration, temperature, and time after induction) on the expression yield and productivity of soluble FGF23 in Rosetta(DE3)/pET22b-SUMO-FGF23. The results showed that, except for the combination of pET22b-SUMO-FGF23 and pET3c-SUMO-FGF23, the two kinds of plasmid, and the Rosetta(DE3) host strain (Fig. 3a) , all other combinations had no target protein expressed. Concerning optimal cell growth conditions for protein production, we screened for suitable IPTG concentration, temperature, and time after induction for the expression yield and productivity of soluble FGF23 in Rosetta(DE3)/ pET22b/SUMO-FGF23. High-level expression and purification of soluble recombinant FGF21 protein by SUMO fusion in Escherichia coli	./cache/cord-004592-a3k56ulv.txt	./txt/cord-004592-a3k56ulv.txt